Anopheles gambiae lipophorin: Characterization and role in lipid transport to developing oocyte

Atella, Geórgia C.; Silva-Neto, Mário A.C.; Golodne, Daniel M.; Arefin, Shamsul; Shahabuddin, Mohammed

doi:10.1016/j.ibmb.2006.01.019

Cited by 52 publications

(45 citation statements)

References 68 publications

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“…The results of these studies are comparable with those of S. serrata with respect to molecular weight and functional characteristics [56]. It would be of interest to know whether crustacean VgR also facilitates the endocytosis of other hemolymph lipoproteins into the ovary, similar to avian VgRs [59] and insectan lipophorin receptor [60].…”

Section: Vitellogenin Receptors and Yolk Protein Uptakesupporting

confidence: 59%

Mechanisms and control of vitellogenesis in crustaceans

Subramoniam

2010

Fish Sci

166

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Crustaceans produce complex yolk proteins to meet the substrate and energy requirements of embryonic development. Early electron microscopic investigations point to a biphasic yolk synthesis, first within the ovary, followed by heterosynthesis at extra-ovarian sites. Recent advances in molecular techniques have enhanced our understanding of the genetic control of yolk synthesis in crustaceans. Amino acid sequencing of crustacean vitellogenin (Vg) has enabled the elucidation of the cDNA sequence associated with it, the identification of genes, and the examination of their expression patterns in different tissues. Yolk processing in crustaeans involves cleavage of the pro-Vg at consensus sites by subtilisin-like endoproteases within the hepatopancreas, hemolymph and oocytes. The structural elucidation of crustacean yolk proteins, as well as the comparison of amino acid sequences of vitellogenins from various crustacean species, has revealed molecular phylogenetic relationships not only among them but also with other large lipid transfer lipoproteins of disparate function. The combinatorial effects of eyestalk neuropeptides and a variety of trophic hormones achieve the hormonal coordination of molting and reproduction. Biogenic amines secreted by the central nervous system may also play an integrative role by stimulating neuropeptide secretion.

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Section: Vitellogenin Receptors and Yolk Protein Uptakesupporting

confidence: 59%

Mechanisms and control of vitellogenesis in crustaceans

Subramoniam

2010

Fish Sci

166

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“…However, during lipid transfer to Anopheles gambiae oocytes by Lp, lipid accumulation occurs simultaneously with the deposition of the protein moiety inside yolk granules through endocytosis (30). This finding is not in agreement with the general idea of Lp as a reusable shuttle for lipids in insects.…”

Section: Results Results Results Resultsmentioning

confidence: 69%

“…During insect oogenesis, oocytes accumulate large amounts of lipids, which are supplied by means of Lpselective lipid transport (9,30). However, during lipid transfer to Anopheles gambiae oocytes by Lp, lipid accumulation occurs simultaneously with the deposition of the protein moiety inside yolk granules through endocytosis (30).…”

Section: Results Results Results Resultsmentioning

confidence: 99%

Purification, partial characterization and role in lipid transport to developing oocytes of a novel lipophorin from the cowpea weevil, Callosobruchus maculatus

Ximenes

Oliveira

Bittencourt‐Cunha

et al. 2007

Braz J Med Biol Res

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Lipid transport in arthropods is achieved by highly specialized lipoproteins, which resemble those described in vertebrate blood. Here we describe purification and characterization of the lipid-apolipoprotein complex, lipophorin (Lp), from adults and larvae of the cowpea weevil Callosobruchus maculatus. We also describe the Lp-mediated lipid transfer to developing oocytes. Lps were isolated from homogenates of C. maculatus larvae and adults by potassio bromide gradient and characterized with respect to physicochemical properties and lipid content. The weevil Lp (465 kDa) and larval Lp (585 kDa), with hydrated densities of 1.22 and 1.14 g/mL, contained 34 and 56% lipids and 9 and 7% carbohydrates, respectively. In both Lps, mannose was the predominant monosaccharide detected by paper chromatography. SDS-PAGE revealed two apolipoproteins in each Lp with molecular masses of 225 kDa (apolipoprotein-I) and 79 kDa (apolipoprotein-II). The lipids were extracted and analyzed by thinlayer chromatography. The major phospholipids found were phosphatidylserine, phosphatidylcholine and phosphatidylethanolamine in adult Lp, and phosphatidylcholine, phosphatidylethanolamine and sphingomyelin in larval Lp. Hydrocarbons, fatty acids and triacylglycerol were the major neutral lipids found in both Lps. Lps labeled in the protein moiety with radioactive iodine ( 125 I-iodine) or in the lipid moiety with fluorescent lipids revealed direct evidence of endocytic uptake of Lps in live oocytes of C. maculatus.

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“…In non-polarized mammalian cells, this FxNPxY signal is entirely responsible for the rapid internalization of the LDL receptor (Chen et al, 1990;Davis et al, 1986). In most instances the function of this putative endocytic sorting signal has not been directly verified in insects, yet both the vitellogenin and lipophorin receptors internalize bound ligands into the developing oocyte and recycle back to the cell surface (Atella et al, 2006;Rodenburg and Van der Horst, 2005;Seo et al, 2003;Snigirevskaya et al, 1997;Sun et al, 2000). The significant conservation of the key specificity-determining residues and positioning relative to the membrane surface therefore suggests that, as in chordates, invertebrate PTB-domain clathrin-associated sorting proteins (CLASPs) might decode this sorting signal to ensure efficient receptor endocytosis in insect cells.…”

Section: Resultsmentioning

confidence: 99%

Internalization of LDL-receptor superfamily yolk-protein receptors during mosquito oogenesis involves transcriptional regulation of PTB-domain adaptors

Mishra

Jha

Steinhauser

et al. 2008

Journal of Cell Science

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In the anautogenous disease vector mosquitoes Anopheles gambiae and Aedes aegypti, egg development is nutritionally controlled. A blood meal permits further maturation of developmentally repressed previtellogenic egg chambers. This entails massive storage of extraovarian yolk precursors by the oocyte, which occurs through a burst of clathrin-mediated endocytosis. Yolk precursors are concentrated at clathrin-coated structures on the oolemma by two endocytic receptors, the vitellogenin and lipophorin receptors. Both these mosquito receptors are members of the low-density-lipoprotein-receptor superfamily that contain FxNPxY-type internalization signals. In mammals, this tyrosine-based signal is not decoded by the endocytic AP-2 adaptor complex directly. Instead, two functionally redundant phosphotyrosine-binding domain adaptors, Disabled 2 and the autosomal recessive hypercholesterolemia protein (ARH) manage the internalization of the FxNPxY sorting signal. Here, we report that a mosquito ARH-like protein, which we designate trephin, possess similar functional properties to the orthologous vertebrate proteins despite engaging AP-2 in an atypical manner, and that mRNA expression in the egg chamber is strongly upregulated shortly following a blood meal. Temporally regulated trephin transcription and translation suggests a mechanism for controlling yolk uptake when vitellogenin and lipophorin receptors are expressed and clathrin coats operate in previtellogenic ovaries.

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Anopheles gambiae lipophorin: Characterization and role in lipid transport to developing oocyte

Cited by 52 publications

References 68 publications

Mechanisms and control of vitellogenesis in crustaceans

Mechanisms and control of vitellogenesis in crustaceans

Purification, partial characterization and role in lipid transport to developing oocytes of a novel lipophorin from the cowpea weevil, Callosobruchus maculatus

Internalization of LDL-receptor superfamily yolk-protein receptors during mosquito oogenesis involves transcriptional regulation of PTB-domain adaptors

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